Electronic Resource
Spatially Resolved Molecular Approaches for the Characterisation of Non-Invasive Follicular Tumours with Papillary-like Features (NIFTPs)
| العنوان: | Spatially Resolved Molecular Approaches for the Characterisation of Non-Invasive Follicular Tumours with Papillary-like Features (NIFTPs) |
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| المؤلفون: | Piga, I, L'Imperio, V, Principi, L, Bellevicine, C, Fusco, N, Maffini, F, Venetis, K, Ivanova, M, Seminati, D, Casati, G, Pagani, L, Galimberti, S, Capitoli, G, Garancini, M, Gatti, A, Magni, F, Pagni, F, Piga, Isabella, L'Imperio, Vincenzo, Principi, Lucrezia, Bellevicine, Claudio, Fusco, Nicola, Maffini, Fausto, Venetis, Konstantinos, Ivanova, Mariia, Seminati, Davide, Casati, Gabriele, Pagani, Lisa, Galimberti, Stefania, Capitoli, Giulia, Garancini, Mattia, Gatti, Andrea-Valer, Magni, Fulvio, Pagni, Fabio |
| بيانات النشر: | MDPI country:CH 2023 |
| نوع الوثيقة: | Electronic Resource |
| مستخلص: | Noninvasive follicular thyroid neoplasms with papillary-like nuclear features (NIFTP) are low-risk thyroid lesions most often characterised by RAS-type mutations. The histological diagnosis may be challenging, and even immunohistochemistry and molecular approaches have not yet provided conclusive solutions. This study characterises a set of NIFTPs by Matrix-Assisted Laser Desorption/Ionisation (MALDI)-Mass Spectrometry Imaging (MSI) to highlight the proteomic signatures capable of overcoming histological challenges. Archived formalin-fixed paraffin-embedded samples from 10 NIFTPs (n = 6 RAS-mutated and n = 4 RAS-wild type) were trypsin-digested and analysed by MALDI-MSI, comparing their profiles to normal tissue and synchronous benign nodules. This allowed the definition of a four-peptide signature able to distinguish RAS-mutant from wild-type cases, the latter showing proteomic similarities to hyperplastic nodules. Moreover, among the differentially expressed signals, Peptidylprolyl Isomerase A (PPIA, 1505.8 m/z), which has already demonstrated a role in the development of cancer, was found overexpressed in NIFTP RAS-mutated nodules compared to wild-type lesions. These results underlined that high-throughput proteomic approaches may add a further level of biological comprehension for NIFTPs. In the future, thanks to the powerful single-cell detail achieved by new instruments, the complementary NGS-MALDI imaging sequence might be the correct methodological approach to confirm that the current NIFTP definition encompasses heterogeneous lesions that must be further characterised. |
| مصطلحات الفهرس: | MALDI–MSI, NGS, NIFTP, proteomic, thyroid cancer, info:eu-repo/semantics/article |
| URL: | info:eu-repo/semantics/altIdentifier/pmid/36768889 info:eu-repo/semantics/altIdentifier/wos/WOS:000931378000001 volume:24 issue:3 journal:INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES |
| الاتاحة: | Open access content. Open access content info:eu-repo/semantics/openAccess |
| ملاحظة: | ELETTRONICO English |
| Other Numbers: | ITBAO oai:boa.unimib.it:10281/403661 10.3390/ijms24032567 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85147892458 1376720927 |
| المصدر المساهم: | BICOCCA OPEN ARCH From OAIster®, provided by the OCLC Cooperative. |
| رقم الانضمام: | edsoai.on1376720927 |
| قاعدة البيانات: | OAIster |
| الوصف غير متاح. |